The structure of the extracellular domains of human interleukin 11 α-receptor reveals mechanisms of cytokine engagement

Metcalfe R, Aizel K, Zlatic C, Nguyen P, Morton C, Lio D, Cheng H, Dobson R, Parker M, Gooley P, Putoczki T, Griffin M, Journal of Biological Chemistry :jbc.RA119.012351 (2020) DOI

SASDGK2 – Interleukin 11/Interleukin 11 receptor alpha complex

Interleukin-11 receptor subunit alpha
Interleukin 11, N-terminal truncation
MWexperimental 50 kDa
MWexpected 50 kDa
VPorod 84 nm3
log I(s) 9.36×10-3 9.36×10-4 9.36×10-5 9.36×10-6
Interleukin-11 receptor subunit alpha Interleukin 11, N-terminal truncation small angle scattering data  s, nm-1
ln I(s)
Interleukin-11 receptor subunit alpha Interleukin 11, N-terminal truncation Guinier plot ln 9.37×10-3 Rg: 3.3 nm 0 (3.3 nm)-2 s2
(sRg)2I(s)/I(0)
Interleukin-11 receptor subunit alpha Interleukin 11, N-terminal truncation Kratky plot 1.104 0 3 sRg
p(r)
Interleukin-11 receptor subunit alpha Interleukin 11, N-terminal truncation pair distance distribution function Rg: 3.3 nm 0 Dmax: 10.2 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Interleukin-11 receptor subunit alpha Interleukin 11, N-terminal truncation OTHER model

log I(s)
 s, nm-1
Interleukin-11 receptor subunit alpha Interleukin 11, N-terminal truncation DAMMIF model

Synchrotron SAXS data from solutions of the interleukin 11/interleukin 11 receptor alpha complex in 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH 8.5 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Dectris/Pilatus3 S 2M detector at a sample-detector distance of 2.5 m and at a wavelength of λ = 0.1078 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 2.2 mg/ml was injected at a 0.45 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. Six successive 1 second frames were collected through the SEC elution peak of the sample. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Interleukin-11 receptor subunit alpha (IL11RA)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   32.2 kDa
 
UniProt   Q14626 (23-319)
Sequence   FASTA
 
Interleukin 11, N-terminal truncation (IL11)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   18.2 kDa
 
UniProt   A8K3F7 (32-199)
Sequence   FASTA